Molecular interactions

Isothermal Titration Calorimetry (ITC) is a technique used in quantitative biomolecular interaction studies. It works by label-free directly measuring the heat that is either released or absorbed during a binding event enabling accurate determination of binding constants (KD), reaction stoichiometry (n), enthalpy (∆H) and entropy (ΔS). This provides a complete thermodynamic profile of the molecular interaction. ITC goes beyond binding affinities and can elucidate the mechanisms underlying molecular interactions.

This application can be used for studying interactions between:

  • Protein – small molecule
  • Target – drug
  • Enzyme – inhibitor
  • Antibody – antigen
  • Protein – protein
  • Protein – DNA
  • Protein – metal ion

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